Conformation of blood-group and virus receptor glycoproteins from red cells and secretions.
Optical rotatory dispersion of human blood-group and virus receptor glycoproteins from erythrocytes and secretions was studied in the far-ultraviolet. Erythrocyte membrane blood-group glycoproteins, with potent virus receptor activities, contained significant alpha-helical and extended beta conformations, whereas the glycoproteins of secretions were largely disordered. These conclusions were supported by determination of the Moffitt constants (b(0)) and by measurements of circular dichroism.
D000998:Antiviral Agents / Q000032:analysis; D001789:Blood Group Antigens; D002462:Cell Membrane / Q000276:immunology; D004848:Epithelium / Q000378:metabolism; D004912:Erythrocytes / Q000276:immunology*; D005122:Exudates and Transudates / Q000276:immunology; D005260:Female; D006023:Glycoproteins / Q000097:blood*; D006384:Hemagglutination; D006801:Humans; D007120:Immunochemistry; D007519:Isoantigens / Q000032:analysis*; D009905:Optical Rotatory Dispersion; D009975:Orthomyxoviridae / Q000276:immunology; D010048:Ovarian Cysts / Q000276:immunology; D014466:Ultraviolet Rays
D000998:Antiviral Agents; D001789:Blood Group Antigens; D006023:Glycoproteins; D007519:Isoantigens